ID   FAB1_MYCTE              Reviewed;         416 AA.
AC   H8ESN0;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 2.
DT   05-DEC-2018, entry version 31.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1;
DE            EC=2.3.1.41;
DE   AltName: Full=Beta-ketoacyl-ACP synthase 1;
DE            Short=KAS 1;
GN   Name=kasA; OrderedLocusNames=ERDMAN_2470;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/JB.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis
RT   Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA   Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT   "M. tuberculosis intramembrane protease Rip1 controls transcription
RT   through three anti-sigma factor substrates.";
RL   Mol. Microbiol. 77:605-617(2010).
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid
CC       synthesis by the addition to an acyl acceptor of two carbons from
CC       malonyl-ACP. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776,
CC         ChEBI:CHEBI:138651; EC=2.3.1.41;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Repressed by Rip1 and independently by the metal
CC       chelator phenanthroline. {ECO:0000269|PubMed:20545848}.
CC   -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
CC       {ECO:0000305}.
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DR   EMBL; AP012340; BAL66261.1; -; Genomic_DNA.
DR   RefSeq; WP_003411571.1; NZ_KK339487.1.
DR   ProteinModelPortal; H8ESN0; -.
DR   SMR; H8ESN0; -.
DR   EnsemblBacteria; BAL66261; BAL66261; ERDMAN_2470.
DR   KEGG; mtn:ERDMAN_2470; -.
DR   PATRIC; fig|652616.3.peg.2513; -.
DR   KO; K11609; -.
DR   OrthoDB; POG091H018O; -.
DR   BioCyc; MTUB652616:G1HGE-2436-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000007568; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Complete proteome; Cytoplasm;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN         1    416       3-oxoacyl-[acyl-carrier-protein] synthase
FT                                1.
FT                                /FTId=PRO_0000422686.
FT   ACT_SITE    171    171       {ECO:0000250}.
SQ   SEQUENCE   416 AA;  43316 MW;  D2187BE2F0B56C7F CRC64;
     MSQPSTANGG FPSVVVTAVT ATTSISPDIE STWKGLLAGE SGIHALEDEF VTKWDLAVKI
     GGHLKDPVDS HMGRLDMRRM SYVQRMGKLL GGQLWESAGS PEVDPDRFAV VVGTGLGGAE
     RIVESYDLMN AGGPRKVSPL AVQMIMPNGA AAVIGLQLGA RAGVMTPVSA CSSGSEAIAH
     AWRQIVMGDA DVAVCGGVEG PIEALPIAAF SMMRAMSTRN DEPERASRPF DKDRDGFVFG
     EAGALMLIET EEHAKARGAK PLARLLGAGI TSDAFHMVAP AADGVRAGRA MTRSLELAGL
     SPADIDHVNA HGTATPIGDA AEANAIRVAG CDQAAVYAPK SALGHSIGAV GALESVLTVL
     TLRDGVIPPT LNYETPDPEI DLDVVAGEPR YGDYRYAVNN SFGFGGHNVA LAFGRY
//